Biotechnical Genetics of Antibiotic Biosynthesis

Brakhage, Axel A.; Turner, Geoffrey

doi:10.1007/978-3-662-10364-7_16

Cited by 20 publications

(13 citation statements)

References 131 publications

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“…In P. chrysogenum, the last enzyme involved in penicillin biosynthesis (acyl CoA:isopenicillin N-acyltransferase) is targeted to peroxisomes by the PTS1 import signal (ARL at the C-terminus) (Müller et al 1991(Müller et al , 1992, and the peroxisomal localization of this enzyme in the related species A nidulans seems likely (Brakhage and Turner 1995). In this way, the biosynthesis of penicillin and the urate oxidation in A. nidulans could be comparable since both processes require the function of peroxisomal enzymes.…”

Section: Discussionmentioning

confidence: 92%

Characterization of oleate-nonutilizing mutants of Aspergillus nidulans isolated by the 3-amino-1,2,4-triazole positive selection method

Lucas

Valenciano

Domínguez

et al. 1997

Archives of Microbiology

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Conidia of Aspergillus nidulans were mutagenized with ultraviolet light and were incubated on a special selective medium containing the catalase inhibitor 3-amino-1,2,4-triazole. From approximately 5 x 10(7) viable UV-irradiated conidia tested, 423 stable mutants resistant to 3-amino-1,2,4-triazole were recovered, of which 40 were unable to grow on minimal medium with oleic acid as the sole carbon source. These oleate-nonutilizing (Ole-) mutants did not grow on medium with carbon sources requiring functional peroxisomes (oleate, butyrate, acetate, or ethanol), but grew well on medium with carbon sources supposedly not requiring such organelles (glucose, glycerol, l-glutamate, or l-proline). The Ole- mutants carried mutations in one of five nuclear genes affecting acetate utilization: acuJ, acuH, acuE, acuL, and perA. The perA21 strain (DL21) carried a mutation in a gene that is not allelic with any of the known acu loci and displayed a phenotype resembling that described in the Pim- (peroxisome import defective) mutants of Hansenula polymorpha. Hyphae of the perA21 mutant contained a few small peroxisomes with the bulk of peroxisomal enzymes remaining in the 20,000 x g supernatant, but produced wild-type levels of penicillin.

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Section: Discussionmentioning

confidence: 92%

Characterization of oleate-nonutilizing mutants of Aspergillus nidulans isolated by the 3-amino-1,2,4-triazole positive selection method

Lucas

Valenciano

Domínguez

et al. 1997

Archives of Microbiology

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“…have shown that there is a correlation between the proliferation rate of microbodies and the capacity for penicillin production in different strains of P. chrysogenum. A. nidulans, like P. chrysogenum, produces penicillin and contains the enzyme acyltransferase, for which a peroxisomal localization has been suggested (Brakhage and Turner 1995). Since the microbodies could play a role in penicillin biosynthesis of A. nidulans, we studied the ultrastructure of wild-type cells grown under penicillin-inducing conditions to determine the proliferation rate of peroxisomes.…”

Section: Resultsmentioning

confidence: 99%

“…The cultures were incubated on a rotary shaker (250 rpm) at 26°C for 24 h. The mycelia were harvested, washed with 0.8% (w/v) NaCl and transferred to 250-ml Erlenmeyer flasks containing 20 ml of fermentation medium (Brakhage et al 1992) plus 1 µg p-aminobenzoic acid ml -1 . This fermentation medium contains corn steep solids (Sigma), a major component of most penicillin production media, and phenoxyacetic acid (Sigma), which acts as a precursor of penicillin V (Brakhage and Turner 1995). Incubation continued under the same conditions for 48 h. Fresh mycelium was used for electron microscopy methods.…”

Section: Strain and Growth Conditionsmentioning

confidence: 99%

Characterization of Aspergillus nidulans peroxisomes by immunoelectron microscopy

Valenciano

Lucas

Klei

et al. 1998

Archives of Microbiology

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In previous work, we have demonstrated that oleate induces a massive proliferation of microbodies (peroxisomes) in Aspergillus nidulans. Although at a lower level, proliferation of peroxisomes also occurrs in cells growing under conditions that induce penicillin biosynthesis. Here, microbodies in oleate-grown A. nidulans cells were characterized by using several antibodies that recognize peroxisomal enzymes and peroxins in a broad spectrum of eukaryotic organisms such as yeast, and plant, and mammalian cells. Peroxisomes were immunolabeled by anti-SKL and anti-thiolase antibodies, which suggests that A. nidulans conserves both PTS1 and PTS2 import mechanisms. Isocitrate lyase and malate synthase, the two key enzymes of the glyoxylate cycle, were also localized in these organelles. In contrast to reports of Neurospora crassa, our results demonstrate that A. nidulans contains only one type of microbody (peroxisomes) that carry out the glyoxylate cycle and contain 3-ketoacyl-CoA thiolase and proteins with the C-terminal SKL tripeptide.

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“…Cubero and Scazzochio (19) expanded the consensus recognition sequence to 5Ј-SYGGRG-3Ј. However, in all A. nidulans creA mutants tested, glucose still represses the ipnA (ϭpcbC) mRNA (11,26). Deletion of a 29-bp region which is protected by the CreA protein did not alter sucrose repression in A. nidulans (27).…”

Section: Is Carbon Catabolite Regulation Of Penicillin Biosynthesis Mmentioning

confidence: 99%

Molecular Control of Expression of Penicillin Biosynthesis Genes in Fungi: Regulatory Proteins Interact with a Bidirectional Promoter Region

Martı́n

2000

J Bacteriol

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Biotechnical Genetics of Antibiotic Biosynthesis

Cited by 20 publications

References 131 publications

Characterization of oleate-nonutilizing mutants of Aspergillus nidulans isolated by the 3-amino-1,2,4-triazole positive selection method

Characterization of oleate-nonutilizing mutants of Aspergillus nidulans isolated by the 3-amino-1,2,4-triazole positive selection method

Characterization of Aspergillus nidulans peroxisomes by immunoelectron microscopy

Molecular Control of Expression of Penicillin Biosynthesis Genes in Fungi: Regulatory Proteins Interact with a Bidirectional Promoter Region

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